Summary: Staphylococcal/Streptococcal toxin, beta-grasp domain
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Staphylococcal/Streptococcal toxin, beta-grasp domain Provide feedback
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This tab holds annotation information from the InterPro database.
InterPro entry IPR006123
Staphylococcal enterotoxins and streptococcal pyrogenic exotoxins constitute a family of biologically and structurally related toxins produced by Staphylococcus aureus and Streptococcus pyogenes [PUBMED:2679358, PUBMED:2185544]. These toxins share the ability to bind to the major histocompatibility complex proteins of their hosts. A more distant relative of the family is the S. aureus toxic shock syndrome toxin, which shares only a low level of sequence similarity with this group.
All of these toxins share a similar two-domain fold (N and C-terminal domains) with a long alpha-helix in the middle of the molecule, a characteristic beta-barrel known as the "oligosaccharide/oligonucleotide fold" at the N-terminal domain and a beta-grasp motif at the C-terminal domain. Each superantigen possesses slightly different binding mode(s) when it interacts with MHC class II molecules or the T-cell receptor [PUBMED:9514739].
The beta-grasp domain has some structural similarities to the beta-grasp motif present in immunoglobulin-binding domains, ubiquitin, 2Fe-2 S ferredoxin and translation initiation factor 3 as identified by the SCOP database.
|Cellular component||extracellular region (GO:0005576)|
|Biological process||pathogenesis (GO:0009405)|
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Curation and family details
|Author:||Finn RD, Bateman A, Griffiths-Jones SR|
|Number in seed:||41|
|Number in full:||3442|
|Average length of the domain:||99.20 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||42.23 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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There are 7 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Stap_Strp_tox_C domain has been found. There are 211 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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